4RM1
The crystal structure of Y333Q mutant pyridoxal-dependent decarboxylase from Sphaerobacter thermophilus DSM 20745
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016830 | molecular_function | carbon-carbon lyase activity |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0019752 | biological_process | carboxylic acid metabolic process |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016830 | molecular_function | carbon-carbon lyase activity |
| B | 0016831 | molecular_function | carboxy-lyase activity |
| B | 0019752 | biological_process | carboxylic acid metabolic process |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016830 | molecular_function | carbon-carbon lyase activity |
| C | 0016831 | molecular_function | carboxy-lyase activity |
| C | 0019752 | biological_process | carboxylic acid metabolic process |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016830 | molecular_function | carbon-carbon lyase activity |
| D | 0016831 | molecular_function | carboxy-lyase activity |
| D | 0019752 | biological_process | carboxylic acid metabolic process |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PMP B 501 |
| Chain | Residue |
| A | THR351 |
| B | ASP272 |
| B | ALA274 |
| B | ASN301 |
| B | GLN303 |
| B | LLP304 |
| B | HOH723 |
| B | HOH787 |
| A | HOH668 |
| B | MET91 |
| B | GLY150 |
| B | GLY151 |
| B | SER152 |
| B | HIS190 |
| B | GLY245 |
| B | THR247 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 502 |
| Chain | Residue |
| B | LEU136 |
| B | PHE137 |
| B | LEU289 |
| B | GLU293 |
| B | HOH887 |
| B | HOH924 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 503 |
| Chain | Residue |
| B | LEU116 |
| B | GLU117 |
| B | ARG124 |
| B | HOH660 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 504 |
| Chain | Residue |
| B | ALA188 |
| B | ALA189 |
| B | HIS190 |
| B | THR191 |
| B | THR247 |
| B | HOH711 |
| B | HOH835 |
| B | HOH906 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL B 505 |
| Chain | Residue |
| A | HIS353 |
| A | HOH621 |
| A | HOH714 |
| B | HIS353 |
| B | HOH648 |
| B | HOH740 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 501 |
| Chain | Residue |
| A | ARG409 |
| A | ALA417 |
| A | ASP421 |
| A | ARG445 |
| A | GLY447 |
| A | HOH661 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL A 502 |
| Chain | Residue |
| A | PHE137 |
| A | ARG286 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 503 |
| Chain | Residue |
| A | SER186 |
| A | GLU187 |
| A | VAL207 |
| A | PRO209 |
| A | HOH940 |
| site_id | AC9 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PMP C 2000 |
| Chain | Residue |
| C | MET91 |
| C | GLY150 |
| C | GLY151 |
| C | SER152 |
| C | HIS190 |
| C | GLY245 |
| C | THR247 |
| C | ASP272 |
| C | ASN301 |
| C | GLN303 |
| C | LLP304 |
| C | HOH2116 |
| C | HOH2206 |
| C | HOH2302 |
| D | THR351 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL D 501 |
| Chain | Residue |
| C | HIS353 |
| C | HOH2140 |
| D | HIS353 |
| D | HOH654 |
| D | HOH668 |
